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N-BOC-3-AMINOPHENOL 97 is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

13683-93-7

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13683-93-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 13683-93-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,3,6,8 and 3 respectively; the second part has 2 digits, 9 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 13683-93:
(7*1)+(6*3)+(5*6)+(4*8)+(3*3)+(2*9)+(1*3)=117
117 % 10 = 7
So 13683-93-7 is a valid CAS Registry Number.
InChI:InChI=1/C11H15NO3/c1-2-3-7-15-11(14)12-9-5-4-6-10(13)8-9/h4-6,8,13H,2-3,7H2,1H3,(H,12,14)

13683-93-7SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name butyl N-(3-hydroxyphenyl)carbamate

1.2 Other means of identification

Product number -
Other names butyl 3-hydroxycarbanilate

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:13683-93-7 SDS

13683-93-7Relevant academic research and scientific papers

Synthesis and characterization of new inhibitors of cholinesterases based on N-phenylcarbamates: In vitro study of inhibitory effect, type of inhibition, lipophilicity and molecular docking

Vor?áková, Katarína,Májeková, Magdaléna,Horáková, Eva,Drabina, Pavel,Sedlák, Milo?,?těpánková, ?árka

, p. 280 - 289 (2018/04/06)

Based on current treatment of Alzheimer's disease, where the carbamate inhibitor Rivastigmine is used, two series of carbamate derivatives were prepared: (i) N-phenylcarbamates with additional carbamate group (1–12) and (ii) N-phenylcarbamates with monosaccharide moiety (13–24). All compounds were tested for the inhibitory effect on both of the cholinesterases, electric eel acetylcholinesterase (eeAChE) and butyrylcholinesterase from equine serum (eqBChE) and the inhibitory activity (expressed as IC50 values) was compared with that of the established drugs Galanthamine and Rivastigmine. The compounds with two carbamate groups 1–12 revealed higher inhibitory efficiency on both cholinesterases in compared with monosaccharide derived carbamates 13–24 and with Rivastigmine. The significant decrease of inhibitory efficiency on eqBChE (also for eeAChE but in less manner) was observed after deacetalization of monosaccharide. Moreover, the type of inhibitory mechanism of five chosen compounds was studied. It was found, that compounds with two carbamate groups act presumably via a mixed inhibitory mechanism and the compounds with monosaccharide moiety act as non-competitive inhibitors. The lipophilicity of tested compounds was determined using partition coefficient. Specific positions of the inhibitors in the binding sites of cholinesterases were determined using molecular modeling and the results indicate the importance of phenylcarbamate orientation in the catalytic gorges of both enzymes.

Synthesis and structure-activity relationships of new β-adrenoreceptor antagonists. Evidence for the electrostatic requirements for β-adrenoreceptor antagonists

Kettmann,Csollei,Racanska,Svec

, p. 843 - 851 (2007/10/02)

A series of mono- and disubstituted phenoxypropanolamines, structurally related to practolol and acebutolol, has been synthesized and tested for β-adrenoreceptor blocking activity. Structure-activity relationships are discussed. The reasons for the lack of activity of compounds 3n and 4n have also been examined. The results suggest that the negative electrostatic potential above the phenyl ring of phenoxypropanolamines is essential for binding activity and point to the presence of an electropositive residue in the β-adrenoreceptor binding site.

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